Myeloperoxidase: friend and foe

Klebanoff, Seymour J

doi:10.1189/jlb.1204697

Cited by 2,282Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressBioactive Compounds and Antitumor Agents

Myeloperoxidase: friend and foe

Klebanoff, Seymour J·2005·Journal of Leukocyte Biology

DOI 10.1189/jlb.1204697

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Abstract

Neutrophilic polymorphonuclear leukocytes (neutrophils) are highly specialized for their primary function, the phagocytosis and destruction of microorganisms. When coated with opsonins (generally complement and/or antibody), microorganisms bind to specific receptors on the surface of the phagocyte and invagination of the cell membrane occurs with the incorporation of the microorganism into an intracellular phagosome. There follows a burst of oxygen consumption, and much, if not all, of the extra oxygen consumed is converted to highly reactive oxygen species. In addition, the cytoplasmic granules discharge their contents into the phagosome, and death of the ingested microorganism soon follows. Among the antimicrobial systems formed in the phagosome is one consisting of myeloperoxidase (MPO), released into the phagosome during the degranulation process, hydrogen peroxide (H2O2), formed by the respiratory burst and a halide, particularly chloride. The initial product of the MPO-H2O2-chloride system is hypochlorous acid, and subsequent formation of chlorine, chloramines, hydroxyl radicals, singlet oxygen, and ozone has been proposed. These same toxic agents can be released to the outside of the cell, where they may attack normal tissue and thus contribute to the pathogenesis of disease. This review will consier the potential sources of H2O2 for the MPO-H2O2-halide system; the toxic products of the MPO system; the evidence for MPO involvement in the microbicidal activity of neutrophils; the involvement of MPO-independent antimicrobial systems; and the role of the MPO system in tissue injury. It is concluded that the MPO system plays an important role in the microbicidal activity of phagocytes.

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MPO is found predominantly in neutrophils and monocytes and catalyzes the reaction of hydrogen peroxide to produce several reactive species, mainly hypochlorous acid (HOCl).
“MPO is found predominantly in neutrophils and monocytes and catalyzes the reaction of hydrogen peroxide to produce several reactive species, mainly hypochlorous acid (HOCl) (discussed in sect. IVB) (516, 1021).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [516]
MPO, lactoperoxidase, and eosinophil peroxidase are integral components of the immune defense.
“MPO, lactoperoxidase, and eosinophil peroxidase are integral components of the immune defense (516).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [516]
MPO is expressed in neutrophil granulocytes and produces hypohalous acids to carry out its antimicrobial activity.
“The enzyme myeloperoxidase MPO is expressed in neutrophil granulocytes (a subtype of white blood cells) and produces hypohalous acids to carry out its antimicrobial activity [146].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [146]

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“These secondarily-derived products, including hypochlorous acid, hydroxyl radical, chloramines, and singlet oxygen, are effective microbicidal compounds [40-43].”
Background
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Authors: Klebanoff, S. J.
Affiliations: University of Washington (US)
Corresponding author: Klebanoff, Seymour J
Venue: Journal of Leukocyte Biology
Publisher: Oxford University Press (OUP)
Published: 2005-02-02
Volume: 77
Issue: 5
Pages: 598-625
ISSN: 0741-5400 (ISSN-L)
1938-3673
DOI: 10.1189/jlb.1204697
OpenAlex: W2059149560
Cited by: 2,282
References: 510
Citations by year: 2026: 67 · 2025: 77 · 2024: 91 · 2023: 81 · 2022: 115 · 2021: 98 · 2020: 139 · 2019: 120 · 2018: 134 · 2017: 138 · 2016: 117 · 2015: 158 · 2014: 141 · 2013: 140 · 2012: 135
FWCI: 5.95
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: Journal of Leukocyte Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
Keywords: myeloperoxidase, neutrophils, phagocytosis, respiratory burst, hydrogen peroxide, hypochlorous acid, reactive oxygen species, microbicidal activity, tissue damage
MeSH terms: Animals, Arteriosclerosis, Humans, Hydrogen Peroxide, Lung Diseases, Peroxidase, Neoplasms, Neutrophils, Phagocytosis, Respiratory Burst, Neutrophil Activation

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

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Myeloperoxidase: friend and foe

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Integrity signals

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